6oqw: Difference between revisions
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==E. coli ATP synthase State 3a== | |||
<StructureSection load='6oqw' size='340' side='right'caption='[[6oqw]], [[Resolution|resolution]] 3.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6oqw]] is a 22 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli], [https://en.wikipedia.org/wiki/Escherichia_coli_2-427-07_S4_C3 Escherichia coli 2-427-07_S4_C3], [https://en.wikipedia.org/wiki/Escherichia_coli_O145:NM Escherichia coli O145:NM], [https://en.wikipedia.org/wiki/Escherichia_coli_Xuzhou21 Escherichia coli Xuzhou21] and [https://en.wikipedia.org/wiki/Escherichia_coli_chi7122 Escherichia coli chi7122]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OQW FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6oqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oqw OCA], [https://pdbe.org/6oqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oqw RCSB], [https://www.ebi.ac.uk/pdbsum/6oqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oqw ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ATPD_ECOLI ATPD_ECOLI] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.[HAMAP-Rule:MF_01416] This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.[HAMAP-Rule:MF_01416] | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: Escherichia coli]] | |||
[[Category: Escherichia coli 2-427-07_S4_C3]] | |||
[[Category: Escherichia coli O145:NM]] | |||
[[Category: Escherichia coli Xuzhou21]] | |||
[[Category: Escherichia coli chi7122]] | |||
[[Category: Large Structures]] | |||
[[Category: Sobti M]] | |||
[[Category: Stewart AG]] | |||
[[Category: Walshe JL]] | |||
Latest revision as of 12:25, 20 March 2024
E. coli ATP synthase State 3aE. coli ATP synthase State 3a
Structural highlights
FunctionATPD_ECOLI F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.[HAMAP-Rule:MF_01416] This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.[HAMAP-Rule:MF_01416] See Also |
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